[1]	NUCLEOTIDE SEQUENCE [MRNA]. PubMed=2753900 [NCBI, ExPASy, EBI, Israel, Japan] Dunn T.J., Koleske A.J., Lindahl R., Pitot H.C.; "Phenobarbital-inducible aldehyde dehydrogenase in the rat. cDNA sequence and regulation of the mRNA by phenobarbital in responsive rats."; J. Biol. Chem. 264:13057-13065(1989).
[2]	FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND TISSUE SPECIFICITY. DOI=10.1021/bi001120m; PubMed=10998257 [NCBI, ExPASy, EBI, Israel, Japan] Kathmann E.C., Naylor S., Lipsky J.J.; "Rat liver constitutive and phenobarbital-inducible cytosolic aldehyde dehydrogenases are highly homologous proteins that function as distinct isozymes."; Biochemistry 39:11170-11176(2000).

Comments

FUNCTION: Can oxidize benzaldehyde, propionaldehyde and acetaldehyde. No detectable activity with retinal.
CATALYTIC ACTIVITY: An aldehyde + NAD⁺ + H₂O = an acid + NADH.

BIOPHYSICOCHEMICAL PROPERTIES:

Kinetic parameters:	K_M=2.4 mM for acetaldehyde;
	K_M=1.6 mM for propionaldehyde;
	K_M=4.7 µM for benzaldehyde;
	Note=The highest catalytic efficiency is observed with benzaldehyde as substrate. No activity with retinal;

PATHWAY: Alcohol metabolism; ethanol degradation; acetate from ethanol: step 2/2 .
SUBUNIT: Homotetramer.
SUBCELLULAR LOCATION: Cytoplasm.
TISSUE SPECIFICITY: Very low levels in lung and liver.
INDUCTION: By phenobarbital.
SIMILARITY: Belongs to the aldehyde dehydrogenase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M23995; AAA40718.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

A32616; A32616.

NP_058968.14; -.

3D structure databases

HSSP

P51977; 1BXS. [HSSP ENTRY / PDB]

ModBase

P13601.

Organism-specific databases

RGD

620252; Aldh1a7.

Family and domain databases

InterPro

IPR016160; Ald_DHase_CS.
IPR016162; Ald_DHase_N.
IPR015590; Aldehyde_DHase.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1.

PANTHER

PTHR11699; Aldehyde_dehyd; 1.

Pfam

PF00171; Aldedh; 1.
Pfam graphical view of domain structure.

PROSITE

PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PS00687; ALDEHYDE_DEHYDR_GLU; 1.

BLOCKS

P13601.

Genome annotation databases

KEGG

rno:29651; -.

Phylogenomic databases

HOVERGEN

P13601; -.

Other

ProtoNet

P13601.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Cytoplasm; NAD; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed (By similarity).`
`CHAIN`	`2 501`	`500`	`Aldehyde dehydrogenase, cytosolic 1.`	`PRO_0000056426`
`NP_BIND`	`246 251`	`6`	`NAD (By similarity).`
`ACT_SITE`	`269 269`		`Proton acceptor (By similarity).`
`ACT_SITE`	`303 303`		`Nucleophile (By similarity).`
`SITE`	`170 170`	`1`	`Transition state stabilizer (By similarity).`

Sequence information

Length: 501 AA [This is the length of the unprocessed precursor]

Molecular weight: 54560 Da [This is the MW of the unprocessed precursor]

CRC64: E6806A1AF736AF1F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSSPAQPAVP APLANLKIQH TKIFINNEWH NSLNGKKFPV INPATEEVIC HVEEGDKADV 

        70         80         90        100        110        120 
DKAVKAARQA FQIGSPWRTM DASERGCLLN KLADLMERDR VLLATMESMN AGKIFTHAYL 

       130        140        150        160        170        180 
LDTEVSIKAL KYFAGWADKI HGQTIPSDGD VFTYTRREPI GVCGQIIPWN GPLILFIWKI 

       190        200        210        220        230        240 
GAALSCGNTV IVKPAEQTPL TALYMASLIK EAGFPPGVVN VVPGYGSTAG AAISSHMDID 

       250        260        270        280        290        300 
KVSFTGSTEV GKLIKEAAGK SNLKRVTLEL GGKSPCIVFA DADLDSAVEF AHQGVFFHQG 

       310        320        330        340        350        360 
QICVAASRLF VEESIYDEFV RRSVERAKKY VLGNPLDSGI SQGPQIDKEQ HAKILDLIES 

       370        380        390        400        410        420 
GKKEGAKLEC GGGRWGNKGF FVQPTVFSNV TDEMRIAKEE IFGPVQQIMK FKSIDEVIKR 

       430        440        450        460        470        480 
ANNTPYGLAA GVFTKDLDRA ITVSSALQAG TVWVNCYLTL SVQCPFGGFK MSGNGREMGE 

       490        500 
QGVYEYTELK TVAMKISQKN S

P13601 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools